Evidence map›Paper›PMID 29882622›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Complete Switch of Reaction Specificity of an Aldolase by Directed Evolution In Vitro: Synthesis of Generic Aliphatic Aldol Products.

Sebastian Junker, Raquel Roldan, Henk-Jan Joosten, Pere Clapés, Wolf-Dieter Fessner

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 41 citations in OpenAlex.

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  8. Biocatalysis: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2021
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Sebastian JunkerInstitut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 4, 64287, Darmstadt, Germany.
Raquel RoldanInstituto de Química Avanzada de Cataluña-IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain.
Henk-Jan JoostenBio-Prodict, Nieuwe Marktstraat 54e, 6511, AA, Nijmegen, The Netherlands.
Pere ClapésInstituto de Química Avanzada de Cataluña-IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain.
Wolf-Dieter FessnerInstitut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 4, 64287, Darmstadt, Germany.ORCID 0000-0002-9787-0752
Institute of Advanced Chemistry of Catalonia · ESTechnische Universität Darmstadt · DEBio-Prodict (Netherlands) · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A structure-guided engineering of fructose-6-phosphate aldolase was performed to expand its substrate promiscuity toward aliphatic nucleophiles, that is, unsubstituted alkanones and alkanals. A "smart" combinatorial library was created targeting residues D6, T26, and N28, which form a binding pocket around the nucleophilic carbon atom. Double-selectivity screening was executed by high-performance TLC that allowed simultaneous determination of total activity as well as a preference for acetone versus propanal as competing nucleophiles. D6 turned out to be the key residue that enabled activity with non-hydroxylated nucleophiles. Altogether 25 single- and double-site variants (D6X and D6X/T26X) were discovered that show useful synthetic activity and a varying preference for ketone or aldehyde as the aldol nucleophiles. Remarkably, all of the novel variants had completely lost their native activity for cleavage of fructose 6-phosphate.

Indexed as

Crystallography, X-RayFructose-Bisphosphate AldolaseKetonesModels, MolecularMolecular StructureFructose-Bisphosphate AldolaseKetonesbiocatalysisfructose-6-phosphate aldolaseHPTLC screeningprotein engineeringstereoselectivity

Identifiers

PMID29882622
PMCPMC6099348
OpenAlexW2807574667

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.